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P0A7P5 (RL34_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L34
Gene names
Name:rpmH
Synonyms:rimA, ssaF
Ordered Locus Names:b3703, JW3680
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length46 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L34P family.

Mass spectrometry

Molecular mass is 5380.5 Da from positions 1 - 46. Determined by MALDI. Ref.7

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionstructural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464650S ribosomal protein L34 HAMAP-Rule MF_00391
PRO_0000187377

Secondary structure

1 ......... 46
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7P5 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 600916E398939412

FASTA465,380
        10         20         30         40 
MKRTFQPSVL KRNRSHGFRA RMATKNGRQV LARRRAKGRA RLTVSK

« Hide

References

« Hide 'large scale' references
[1]"The sequence determination of a protein in a micro scale: the sequence analysis of ribosomal protein L34 of Escherichia coli."
Chen R.
Hoppe-Seyler's Z. Physiol. Chem. 357:873-886(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K12.
[2]"The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH gene, coding for the ribosomal protein L34, of Escherichia coli."
Hansen F.G., Hansen E.B., Atlung T.
EMBO J. 1:1043-1048(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Physical mapping and nucleotide sequence of the rnpA gene that encodes the protein component of ribonuclease P in Escherichia coli."
Hansen F.G., Hansen E.B., Atlung T.
Gene 38:85-93(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
Arnold R.J., Reilly J.P.
Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[8]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01602 Genomic DNA. Translation: AAB59148.1.
X01861 Genomic DNA. Translation: CAA25982.1.
M11056 Genomic DNA. Translation: AAA24566.1.
L10328 Genomic DNA. Translation: AAA62054.1.
U00096 Genomic DNA. Translation: AAC76726.1.
AP009048 Genomic DNA. Translation: BAE77591.1.
RefSeqNP_418158.1. NC_000913.3.
YP_491732.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.4621-46[»]
1VS8X-ray3.4621-46[»]
1VT2X-ray3.3021-46[»]
2AW4X-ray3.4621-46[»]
2AWBX-ray3.4621-46[»]
2I2TX-ray3.2221-46[»]
2I2VX-ray3.2221-46[»]
2J28electron microscopy8.0021-46[»]
2QAMX-ray3.2121-46[»]
2QAOX-ray3.2121-46[»]
2QBAX-ray3.5421-46[»]
2QBCX-ray3.5421-46[»]
2QBEX-ray3.3021-46[»]
2QBGX-ray3.3021-46[»]
2QBIX-ray4.0021-46[»]
2QBKX-ray4.0021-46[»]
2QOVX-ray3.9321-46[»]
2QOXX-ray3.9321-46[»]
2QOZX-ray3.5021-46[»]
2QP1X-ray3.5021-46[»]
2RDOelectron microscopy9.1021-46[»]
2VHMX-ray3.7421-46[»]
2VHNX-ray3.7421-46[»]
2WWQelectron microscopy5.8061-46[»]
2Z4LX-ray4.4521-46[»]
2Z4NX-ray4.4521-46[»]
3BBXelectron microscopy10.0021-46[»]
3DF2X-ray3.5021-46[»]
3DF4X-ray3.5021-46[»]
3E1Belectron microscopy-V1-46[»]
3E1Delectron microscopy-V1-46[»]
3FIKelectron microscopy6.7021-46[»]
3I1NX-ray3.1921-46[»]
3I1PX-ray3.1921-46[»]
3I1RX-ray3.8121-46[»]
3I1TX-ray3.8121-46[»]
3I20X-ray3.7121-46[»]
3I22X-ray3.7121-46[»]
3IZTelectron microscopy-e1-46[»]
3IZUelectron microscopy-e1-46[»]
3J01electron microscopy-21-46[»]
3J0Telectron microscopy12.1051-46[»]
3J0Welectron microscopy14.7051-46[»]
3J0Yelectron microscopy13.5051-46[»]
3J11electron microscopy13.1051-46[»]
3J12electron microscopy11.5051-46[»]
3J14electron microscopy11.5051-46[»]
3J19electron microscopy8.3021-46[»]
3J37electron microscopy9.8071-46[»]
3J4Xelectron microscopy12.0021-46[»]
3J50electron microscopy20.0021-46[»]
3J51electron microscopy17.0021-46[»]
3J52electron microscopy12.0021-46[»]
3J54electron microscopy13.0021-46[»]
3J56electron microscopy15.0021-46[»]
3J58electron microscopy17.0021-46[»]
3J5Aelectron microscopy12.0021-46[»]
3J5Celectron microscopy17.0021-46[»]
3J5Eelectron microscopy17.0021-46[»]
3J5Gelectron microscopy20.0021-46[»]
3J5Ielectron microscopy15.0021-46[»]
3J5Kelectron microscopy9.0021-46[»]
3J5Lelectron microscopy6.6021-46[»]
3J5Oelectron microscopy6.8021-46[»]
3J5Uelectron microscopy7.6051-46[»]
3J5Welectron microscopy7.6061-46[»]
3KCRelectron microscopy-21-46[»]
3OASX-ray3.2521-46[»]
3OATX-ray3.2521-46[»]
3OFCX-ray3.1921-46[»]
3OFDX-ray3.1921-46[»]
3OFQX-ray3.1021-46[»]
3OFRX-ray3.1021-46[»]
3OFZX-ray3.2921-46[»]
3OG0X-ray3.2921-46[»]
3ORBX-ray3.3021-46[»]
3R8SX-ray3.0021-46[»]
3R8TX-ray3.0021-46[»]
3SGFX-ray3.2061-46[»]
3UOSX-ray3.7061-46[»]
4GARX-ray3.3021-46[»]
4GAUX-ray3.3021-46[»]
4KIXX-ray2.9021-46[»]
4KIZX-ray2.9021-46[»]
4KJ1X-ray2.9021-46[»]
4KJ3X-ray2.9021-46[»]
4KJ5X-ray2.9021-46[»]
4KJ7X-ray2.9021-46[»]
4KJ9X-ray2.9021-46[»]
4KJBX-ray2.9021-46[»]
ProteinModelPortalP0A7P5.
SMRP0A7P5. Positions 3-43.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-581N.
IntActP0A7P5. 3 interactions.
STRING511145.b3703.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7P5.
PRIDEP0A7P5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76726; AAC76726; b3703.
BAE77591; BAE77591; BAE77591.
GeneID12930542.
948216.
KEGGecj:Y75_p3470.
eco:b3703.
PATRIC32122903. VBIEscCol129921_3827.

Organism-specific databases

EchoBASEEB0885.
EcoGeneEG10892. rpmH.

Phylogenomic databases

eggNOGCOG0230.
HOGENOMHOG000111572.
KOK02914.
OrthoDBEOG6DZF71.
PhylomeDBP0A7P5.

Enzyme and pathway databases

BioCycEcoCyc:EG10892-MONOMER.
ECOL316407:JW3680-MONOMER.

Gene expression databases

GenevestigatorP0A7P5.

Family and domain databases

HAMAPMF_00391. Ribosomal_L34.
InterProIPR000271. Ribosomal_L34.
IPR020939. Ribosomal_L34_CS.
[Graphical view]
PANTHERPTHR14503. PTHR14503. 1 hit.
PfamPF00468. Ribosomal_L34. 1 hit.
[Graphical view]
ProDomPD003101. Ribosomal_L34. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01030. rpmH_bact. 1 hit.
PROSITEPS00784. RIBOSOMAL_L34. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7P5.
PROP0A7P5.

Entry information

Entry nameRL34_ECOLI
AccessionPrimary (citable) accession number: P0A7P5
Secondary accession number(s): P02437, Q2M815
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents